EIF3A_DEBHA
ID EIF3A_DEBHA Reviewed; 900 AA.
AC B5RUP5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
GN OrderedLocusNames=DEHA2G10098g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR382139; CAR65939.1; -; Genomic_DNA.
DR RefSeq; XP_002770604.1; XM_002770558.1.
DR AlphaFoldDB; B5RUP5; -.
DR SMR; B5RUP5; -.
DR STRING; 4959.XP_002770604.1; -.
DR EnsemblFungi; CAR65939; CAR65939; DEHA2G10098g.
DR GeneID; 8999161; -.
DR KEGG; dha:DEHA2G10098g; -.
DR VEuPathDB; FungiDB:DEHA2G10098g; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; B5RUP5; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
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 SMART; SM00088; PINT; 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..900
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366361"
FT DOMAIN 326..508
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 808..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..129
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 551..859
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 808..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 103683 MW; 626C44D61C40643A CRC64;
MAPPHRHHNF RPENVYKRAE DLIAVGQRNA ALETLYELIT SKRIRYLAVQ DLEPIALLLI
ELAVDLRKGK LAKDALHQYK KNVQLSENGL ESVQVIVRKF IELAEKKLEE AQAKADVKID
QGEVEDLEAA QTPESILLSA VSNADSADRT ERELVNPWLR FLWEALRAVL DILRNNSKLE
VTYSAIVNQA FQFCLKFNRK AEFRRLCELL RGHMQSVTTQ IKPTGSMNAI DLSDSETVQR
YLDQRFAQLN ISVKLELWQE SFRSVDDVHT LITASKKAPR PVMMANYYEN LGRIFAVSGN
SLYHAAAWNK FFNLYCQSPN ATDDELSHYA SILVLATLSV PQKSLNSNET VVDDHKAKNA
KLTSLLNLNQ VPTRDTLLKS IVSRSILSFV DPAVKQLFTV LEEDEFHPLT IKKKVSEVFQ
LIESNKDYKQ YIPTLTEAIL IRLYQQVSQV YETVKLDFLV SLGIIEGTEF SLSALEVENL
IVNGVKDGHL SLTIDHETDV VTLKSKPFED AFTDSLTSKL QISPSELVRS QLSKLAQTLS
SSAKVIDPEY EVRIQKTRNE ALKNAIADMA REQQEIADRV NVMEERKRIA DKAKREQDEE
AARLRQEANV AEQKAEQERI LAEQERRNLE KLERERQLVK EKEKLKIAEE INAKGIIKLD
LNNLDDLDTE KLRIMQIEQL NKDKKDLEER LKVLSKKNDH TERAFRRYEL QYLEKDAEKQ
QEDDIKNYET LKELKISKAK KDHEESLALK DRLQRIVPDF EPFKKIIDEK HSSKLAELRK
EAQAALEQAK RERTERVKHQ RMDELMERRE YERKEAEQEE IKRKRQEEMD KFKEELRIQK
EKDADSLRRR QEMANESAKP ATPEPVPAPV PAAAAAAAKP SAPLTFAEKM RLKRLGKPGN
