EIF3A_YARLI
ID EIF3A_YARLI Reviewed; 955 AA.
AC Q6C161;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=YALI0F18942g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382132; CAG78410.1; -; Genomic_DNA.
DR RefSeq; XP_505601.1; XM_505601.1.
DR AlphaFoldDB; Q6C161; -.
DR SMR; Q6C161; -.
DR STRING; 4952.CAG78410; -.
DR EnsemblFungi; CAG78410; CAG78410; YALI0_F18942g.
DR GeneID; 2909029; -.
DR KEGG; yli:YALI0F18942g; -.
DR VEuPathDB; FungiDB:YALI0_F18942g; -.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; Q6C161; -.
DR OMA; VMYQTTA; -.
DR Proteomes; UP000001300; Chromosome F.
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: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 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..955
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366371"
FT DOMAIN 325..498
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 789..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 533..636
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 752..860
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 789..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 107121 MW; EEB9399A19A64B42 CRC64;
MAPHQNVRPE TVLKRTDELI AVGQQDAALE LLHETVSARK ARTTSVATLE PIVARFVQLS
VDLRKGKIIK DGLHQYKKIV QSTNVNAIEP VIKQFLSLAE QRVTDAQAQA DKIADEEEAD
DLEAEETPED LLLATVSSED TKDRTDRRVV TPWLKFLWEA YRSVLDVLRN NSKLEVIYQQ
VVEQAFNFCL KFSRKTEFRR LCELLRSHLQ TTAQKGPNAP PVTATSVDLS DADTLQRYLD
TRFSQLNVAV KLELWQEAFR SVEDVHTLLT VSKRPAKPLM MGNYYENLAR IFLVAGNYLF
HAAAWNKLFH LLSQSPRGAI PVSEYQRVAS FVLLSALAIP HNSSAEDRYR NTRLTGLLNL
QRTPTRDALL KSALSRNILA HVKPEIKALY KTLEVDFHPL SIRAKLTPVV GAIAEAPEFK
PYFAPLYQVI LTRLFQQLSQ VYESVKLDFV IQLATFPAPF SATPLEIEQF IVRACAQGEL
AIKIDHDQRS VLFEEVRAAT GSASLQDTPI EIVRTQLSRL GRTLSVADPL NSAEAREQQY
VAALTTAQDN AEREHAETLA RRAEIEARKA QAEAERAQRE EEEARKRAQR LLDEELAEKE
RLAAEQHARE LERIRKEQDA IREEEKKKLA EEINAKGIIT IDLDKLEGLD TNALRKMQVD
QLAKETKELG DRLRVTARRI DHTERAYRME EIKLVEDDFV KQKQRDREIY DTRIKLIKDT
AKAEHDAKVE LAKRLQRAVP FYKSFRDDIR VKREAEFTRL REEAVKNLAE AKAARIEEVK
AKRIADAKRA EEEAKAAAEA EAKAAAEAEA KAKAEQEMRE KLLAEKKARE EANARADAAY
EKQRQKEAEL EAKLEAKRAG FSGAGRQAPP SGGYVPPSRR EGGYVPPSRR GDAGAAPGAG
SGGYTPPSRR EGGGGGYVPP SRREGGGGGY VPPSRREGGS GAGSGGRYIP PSQRN
